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Plant Physiology 88:245-247 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Cytokinin Oxidase from Phaseolus vulgaris Callus Cultures 1

Affinity for Concanavalin

J. Mark Chatfield2 and Donald J. Armstrong

Department of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331

Cytokinin oxidase activity from Phaseolus vulgaris cv Great Northern callus cultures exhibited affinity for the lectin concanavalin A. Over 80% of the activity extracted from the callus tissue bound to a concanavalin A-Sepharose 4B column. The bound activity was eluted from the column by the addition of methylmannose to the eluting buffer. On the basis of this result, it appears that most of the cyokinin oxidase activity present in Great Northern callus cultures exists in the form of a glycoprotein. The apparent pI of this enzyme, as estimated by chromatofocusing, is approximately 5.0.


2 Present address: USDA/ARS, Department of Agronomy, University of Illinois, Urbana, IL 61801.

1 Supported by the Science and Education Administration of the United States Department of Agriculture under Grant 86-CRCR-1-1988 from the Competitive Research Grants Office.




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K. D. Bilyeu, J. L. Cole, J. G. Laskey, W. R. Riekhof, T. J. Esparza, M. D. Kramer, and R. O. Morris
Molecular and Biochemical Characterization of a Cytokinin Oxidase from Maize
Plant Physiology, January 1, 2001; 125(1): 378 - 386.
[Abstract] [Full Text]




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Copyright © 1988 by the American Society of Plant Biologists